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Acid Peptide (acid + peptide)
Kinds of Acid Peptide Selected AbstractsCover Picture: Electrophoresis 2'2010ELECTROPHORESIS, Issue 2 2010Article first published online: 18 JAN 2010 Issue no. 2 has 19 contributions including one Fast Track contribution on "Thermophoresis of ssDNA". The remaining 18 articles cover a wide variety of investigation involving nucleic acids, cells, viruses, interactive CE, detection methodologies in CE, enantioseparations, and studies on proteins and proteomics. Further selected articles include: Capillary electrophoresis of bone marrow stromal cells with uptake of heparin-functionalized poly(lactide-co-glycolide) nanoparticles during differentiation towards neurons. ((10.1002/elps.200900336)) Ghrelin-liposome interactions. Characterization of liposomal formulations of an acylated 28-amino acid peptide using capillary electrophoresis. ((10.1002/elps.200900394)) [source] Differences in the skin peptides of the male and female Australian tree frog Litoria splendidaFEBS JOURNAL, Issue 1 2000The discovery of the aquatic male sex pheromone splendipherin, a new antibiotic peptide caerin 1.10, together with Phe8 caerulein The skin secretions of female and male Litoria splendida have been monitored monthly over a three-year period using HPLC and electrospray mass spectrometry. Two minor peptides are present only in the skin secretion of the male. The first of these is the female-attracting aquatic male sex pheromone that we have named splendipherin, a 25 amino acid peptide (GLVSSIGKALGGLLADVVKSKGQPA-OH). This pheromone constitutes about 1% of the total skin peptides during the breeding season (January to March), dropping to about 0.1% during the period June to November. Splendipherin attracts the female in water at a concentration of 10,11,10,9 m, and is species specific. The second peptide is a wide-spectrum antibiotic of the caerin 1 group, a 25 residue peptide (GLLSVLGSVAKHVLPHVVPVIAEKL-NH2) named caerin 1.10. The neuropeptides of L. splendida are also seasonally variable, the change identical for both the female and male. During the period October to March, the sole neuropeptide present in skin secretions is caerulein [pEQDY(SO3)TGWMDF-NH2]; this is active on smooth muscle and is also an analgaesic. During the southern winter (June to September), more than half of the caerulein is hydrolysed to [pEQDYTGWMDF-NH2], a peptide that shows no smooth muscle activity. In place of caerulein, a new peptide, Phe8 caerulein [pEQDY(SO3)TGWFDF-NH2], becomes a major component of the skin secretion. Perhaps this seasonal change is involved in thermoregulation, that is, with the initiation and maintenance of the inactive (hibernation) phase of the animal. [source] Vasoactive intestinal peptide acts via multiple signal pathways to regulate hippocampal NMDA receptors and synaptic transmissionHIPPOCAMPUS, Issue 9 2009Kai Yang Abstract Vasoactive intestinal peptide (VIP) is a 28-amino acid peptide, which belongs to a superfamily of structurally related peptide hormones including pituitary adenylate cyclase-activating polypeptide (PACAP). Although several studies have identified the involvement of PACAP in learning and memory, little work has been done to investigate such a role for VIP. At least three receptors for VIP have been identified including the PACAP receptor (PAC1-R) and the two VIP receptors (VPAC receptors). VIP can activate the PAC1-R only if it is used at relatively high concentrations (e.g., 100 nM); however, at lower concentrations (e.g., 1 nM) it is selective for the VPAC receptors. Our lab has showed that PAC1-R activation signals through PKC/CAK,/Src pathway to regulate NMDA receptors; however, there is little known about the potential regulation of NMDA receptors by VPAC receptors. Our studies demonstrated that application of 1 nM VIP enhanced NMDA currents by stimulating the VPAC receptors as the effect was blocked by VPAC receptor antagonist [Ac-Tyr1, D-Phe2]GRF (1,29). This enhancement of NMDA currents was blocked by both Rp-cAMPS and PKI14,22 (they are highly specific PKA inhibitors), but not by the specific PKC inhibitor, bisindolylmaleimide I. In addition, the VIP-induced enhancement of NMDA currents was accentuated by inhibition of phosphodiesterase 4, which inhibits the degradation of cAMP. This regulation of NMDA receptors also required the scaffolding protein AKAP. In contrast, the potentiation induced by high concentration of VIP (e.g., 100 nM) was mediated by PAC1-R as well as by Src kinase. Overall, these results show that VIP can regulate NMDA receptors through different receptors and signaling pathways. © 2009 Wiley-Liss, Inc. [source] Analysis of a late gene, orf101 from Helicoverpa armigera single nucleocapsid nucleopolyhedrovirusINSECT SCIENCE, Issue 5 2005SHI-HENG AN Abstract Helicoverpa armigera single nucleocapsid nucleopolyhedrovirus open reading frame 101 (ha101) is 762 nts in length and encodes a 254 amino acid peptide with predicted 29 kDa molecular weight. The homologues of ha101 were explored using BLASTP searching tool in the updated GenBank/EMBL and SWISS-PROT databases. The results showed that the homologues of ha101 were present in all the completely sequenced lepidopteran nucleopolyhedroviruses and granuloviruses, suggesting that ha101 might be a functional gene associated with their lepidopteran hosts. Sequence alignment of ha101 and its homologues revealed that 10 amino acids were completely conserved. RT-PCR analysis of ha101 manifested that the transcript of ha101 was first detected at 24 hpi and remained detectable at up to 122 hpi, suggesting that ha101 was transcribed during late stages of infection. Ha101 was expressed using Bac to Bac system in Tn5B-1-4 cells. The product of ha101 expressed in Tn5B-1-4 cells was approximately 29 kDa, consistent with the predicted molecular weight, and the results were confirmed by western blot analysis. The subcellular localization indicated that ha101 was aggregated along nuclear envelope during the early stages of infection and spread out to the entire nucleus including virogenic stroma in late stages of infection, suggesting that ha101 may play a specific role in virion assembly process or virogenic stroma arrangement. [source] Leptin and leptin receptor in human seminal plasma and in human spermatozoaINTERNATIONAL JOURNAL OF ANDROLOGY, Issue 6 2003T. Jope Summary Leptin, a 167 amino acid peptide, is known to influence the gonads via direct and indirect effects. Recent studies provide contradictory proposition about the peripheral impact of leptin in the male gonads. Thus, we examined leptin and its receptors in human seminal plasma and in human ejaculated spermatozoa by Western blot technique and fluorescence microscopy. In seminal plasma we found a free leptin band (16 kDa) by an anti-leptin polyclonal antibody. Incubation of seminal plasma with recombinant leptin caused a statistically significant increase in the amount of free leptin (p < 0.01) and supports this finding. Furthermore, a soluble leptin receptor (145 kDa) was found in human seminal plasma in the same specimen. We also detected a 145-kDa leptin receptor isoform in ejaculated spermatozoa as a possible target of leptin action in the male genital tract, which was localized at the tail of spermatozoa by immunofluorescence microscopy only. This receptor was significantly associated with the intactness of sperm plasma membranes. Spermatozoa with deteriorated membranes contained 49.2 ± 6.9% leptin receptor signal intensity compared with spermatozoa having intact membranes (p < 0.01). This finding is difficult to interpret and may be caused by a leakage of OB-R due to loss of membrane integrity. In conclusion, these data provide further hints for a peripheral role of leptin in the male genital tract, possibly, by an interaction between leptin and spermatozoa via sperm leptin receptors. [source] Amylin and Bone Metabolism in Streptozotocin-Induced Diabetic RatsJOURNAL OF BONE AND MINERAL RESEARCH, Issue 5 2001Marie-Noëlle Horcajada-Molteni Abstract Amylin (AMY) is a 37 amino acid peptide cosecreted with insulin (INS) by pancreatic ,-cells and absent in type 1 diabetes, a condition frequently associated with osteopenia. AMY binds to calcitonin receptors, lowers plasma calcium concentration, inhibits osteoclast activity, and stimulates osteoblasts. In the present study, we examined the effects of AMY replacement on bone loss in a streptozotocin (STZ)-induced rodent model type 1 diabetes. Of 50 male Wistar rats studied, 40 were made diabetic with intraperitoneal STZ (50 mg/kg; plasma glucose concentrations >11 mM within 5 days). Ten nondiabetic control (CONT) rats received citrate buffer without STZ. Diabetic rats were divided into four groups (n = 10/group) and injected subcutaneously with rat AMY (45 mg/kg), INS (12 U/kg), both (same doses), or saline (STZ; diabetic controls) once per day. After 40 days of treatment and five 24-h periods of urine collection for deoxypyridinoline (DPD), the animals were killed, blood was sampled, and femurs were removed. The left femur was tested for mechanical resistance (three-point bending). The right femur was tested for total, diaphyseal (cortical bone), and metaphyseal (trabecular bone) bone densities using dual-energy X-ray absorptiometry (DXA). Bone was ashed to determine total bone mineral (calcium) content. None of the treatments had any significant effect on femoral length and diameter. Untreated diabetic rats (STZ; 145 ± 7N) had lower bone strength than did nondiabetic CONT (164 ± 38; p < 0.05). Total bone mineral density (BMD; g/cm2) was significantly lower in STZ (0. 2523 ± 0. 0076) than in CONT (0.2826 ± 0.0055), as were metaphyseal and diaphyseal densities. Diabetic rats treated with AMY, INS, or both had bone strengths and bone densities that were indistinguishable from those in nondiabetic CONT. Changes in bone mineral content paralleled those for total BMD (T-BMD). Plasma osteocalcin (OC) concentration, a marker for osteoblastic activity, was markedly lower in untreated diabetic rats (7. 6 ± 0. 9 ng/ml); p < 0. 05) than in nondiabetic CONT (29. 8 ± 1. 7; p < 0. 05) or than in AMY (20. 1 ± 0. 7; p < 0. 05). Urinary DPD excretion, a marker for bone resorption, was similar in untreated and AMY-treated diabetic rats (35.0 ± 3.1 vs. 35.1 ± 4.4 nmol/mmol creatinine), intermediate in rats treated with INS (49.9 ± 2.7), and normalized in diabetic rats treated with both agents (58.8 ± 8.9 vs. 63.2 ± 4.5 in CONT). Thus, in our STZ rat model of diabetic osteopenia, addition of AMY improved bone indices apparently by both inhibiting resorption and stimulating bone formation. [source] Neuropeptide Y stimulates retinal neural cell proliferation , involvement of nitric oxideJOURNAL OF NEUROCHEMISTRY, Issue 6 2008Ana Rita Álvaro Abstract Neuropeptide Y (NPY) is a 36 amino acid peptide widely present in the CNS, including the retina. Previous studies have demonstrated that NPY promotes cell proliferation of rat post-natal hippocampal and olfactory epithelium precursor cells. The aim of this work was to investigate the role of NPY on cell proliferation of rat retinal neural cells. For this purpose, primary retinal cell cultures expressing NPY, and NPY Y1, Y2, Y4 and Y5 receptors [Álvaro et al., (2007) Neurochem. Int., 50, 757] were used. NPY (10,1000 nM) stimulated cell proliferation through the activation of NPY Y1, Y2 and Y5 receptors. NPY also increased the number of proliferating neuronal progenitor cells (BrdU+/nestin+ cells). The intracellular mechanisms coupled to NPY receptors activation that mediate the increase in cell proliferation were also investigated. The stimulatory effect of NPY on cell proliferation was reduced by l -nitroarginine-methyl-esther (l -NAME; 500 ,M), a nitric oxide synthase inhibitor, 1H-[1,2,4]oxadiazolo-[4, 3-a]quinoxalin-1-one (ODQ; 20 ,M), a soluble guanylyl cyclase inhibitor or U0126 (1 ,M), an inhibitor of the extracellular signal-regulated kinase 1/2 (ERK 1/2). In conclusion, NPY stimulates retinal neural cell proliferation, and this effect is mediated through nitric oxide,cyclic GMP and ERK 1/2 pathways. [source] Full-length bovine spp24 [spp24 (24-203)] inhibits BMP-2 induced bone formation,JOURNAL OF ORTHOPAEDIC RESEARCH, Issue 6 2008Chananit Sintuu Abstract Secreted phosphoprotein 24 kDa (spp24) is a bone matrix protein. It contains a TGF-, receptor II homology 1 (TRH1) domain. A cyclic, synthetic 19 amino acid peptide (bone morphogenetic protein binding peptide or BBP) based on the sequence of the TRH1 domain enhances BMP-2 induced osteogenesis. Many observations suggest that different size forms of this protein have very different effects (inhibiting or enhancing) on BMP-2 induced osteogenesis. Using the stable recombinant Met(His)6 -tagged secretory form of full-length (fl) bovine spp24 [Met(His)6 -spp24 (residues 24,203)] and transgenic (TG) mice expressing fl bovine spp24 (residues 1,203), we have demonstrated that spp24 inhibits BMP-2 induced bone formation. The effects of Met(His)6 -spp24 (24,203) were determined in the ectopic bone-forming bioassay in male mice. Implantation of 5 µg of BMP-2 stimulated bone formation, assessed densitometrically as bone area and mineral content. When Met(His)6 -spp24 (24,203) was implanted with BMP-2, it elicited a dose-dependent decrease in BMP-2-medicated ectopic bone formation. When added at a 50-fold excess (w/w), Met(His)6 -spp24 (24,203) completely ablated the effects of BMP-2, while addition of a 10-fold excess had no effect. Constitutive expression of fl bovine spp24 (1,203) under the control of the osteocalcin promoter in TG female mice reduced femoral and vertebral bone mineral density at 3 months of age and reduced femoral BMD at 8 months of age, but had no effects in male mice, which can exhibit less osteocalcin-promoter driven gene transcription than females. Histomorphometric analysis demonstrated that bone volume and trabecular thickness were lower in TG female mice at 3 months of age than in sex- and age-matched wild type (WT) controls. Thus, fl spp24 and its secretory isoform (Met(His)6 -spp24 [24,203]), which contain a BMP-binding or TRH1 motif, inhibit ectopic bone formation in male mice and adversely affects BMD and histological parameters related to bone mass and formation in female mice expressing the human transgene. Under these conditions, fl spp24 acts as a BMP antagonist in vivo. © 2008 Orthopaedic Society. Published by Wiley Periodicals, Inc. J Orthop Res 26:753,758, 2008 [source] Use of peptide for selective and sensitive detection of an Anthrax biomarker via peptide recognition and surface-enhanced Raman scatteringJOURNAL OF RAMAN SPECTROSCOPY, Issue 2 2010Kyungtag Ryu Abstract A short 16-amino acid peptide has been used in place of an antibody to selectively detect the specific Anthrax biomarker, protective antigen (PA), using surface-enhanced Raman scattering (SERS). Peptides are more stable than antibodies under various biological conditions and are easily synthesized for a specific target. A peptide that has high affinity to PA was conjugated onto gold nanoparticles along with a Raman reporter and then incubated in various concentrations of PA. Parallel studies in which the peptide sequence was replaced with an antibody were performed to compare the performance of the two methodologies. Both the peptide and antibody functionalized nanoparticles were able to specifically detect PA concentrations down to 6.1 fM. These results demonstrate that these short, robust peptides can be used in the place of traditional antibodies to specifically recognize target biomarkers in the field for the potential diagnosis of disease. Copyright © 2010 John Wiley & Sons, Ltd. [source] IR/Raman spectroscopy and DFT calculations of cyclic di-amino acid peptides.JOURNAL OF RAMAN SPECTROSCOPY, Issue 11 2009Part III: comparison of solid state, solution structures of cyclo(L -Ser- L -Ser) Abstract B3-LYP/cc-pVDZ calculations of the gas-phase structure and vibrational spectra of the isolated molecule cyclo(L -Ser- L -Ser), a cyclic di-amino acid peptide (CDAP), were carried out by assuming C2 symmetry. It is predicted that the minimum-energy structure is a boat conformation for the diketopiperazine (DKP) ring with both L -seryl side chains being folded slightly above the ring. An additional structure of higher energy (15.16 kJ mol,1) has been calculated for a DKP ring with a planar geometry, although in this case two fundamental vibrations have been calculated with imaginary wavenumbers. The reported X-ray crystallographic structure of cyclo(L -Ser- L -Ser), shows that the DKP ring displays a near-planar conformation, with both the two L -seryl side chains being folded above the ring. It is hypothesized that the crystal packing forces constrain the DKP ring in a planar conformation and it is probable that the lower energy boat conformation may prevail in the aqueous environment. Raman scattering and Fourier-transform infrared (FT-IR) spectra of solid state and aqueous solution samples of cyclo(L -Ser- L -Ser) are reported and discussed. Vibrational band assignments have been made on the basis of comparisons with the calculated vibrational spectra and band wavenumber shifts upon deuteration of labile protons. The experimental Raman and IR results for solid-state samples show characteristic amide I vibrations which are split (Raman: 1661 and 1687 cm,1, IR: 1666 and 1680 cm,1), possibly due to interactions between molecules in a crystallographic unit cell. The cis amide I band is differentiated by its deuterium shift of ,30 cm,1, which is larger than that previously reported for trans amide I deuterium shifts. A cis amide II mode has been assigned to a Raman band located at 1520 cm,1. The occurrence of this cis amide II mode at a wavenumber above 1500 cm,1 concurs with results of previously examined CDAP molecules with low molecular weight substituents on the C, atoms, and is also indicative of a relatively unstrained DKP ring. Copyright © 2009 John Wiley & Sons, Ltd. [source] Characterization of fibronectin assembly by platelets adherent to adsorbed laminin-111JOURNAL OF THROMBOSIS AND HAEMOSTASIS, Issue 5 2006J. CHO Summary.,Background: Various types of laminin (LN) are ubiquitous components of basement membrane and exposed to blood upon localized damage of vascular endothelial cells. Fibronectin is a plasma protein that is insolubilized into fibrils in a regulated fashion by, for example, lysophosphatidic acid (LPA)-stimulated fibroblasts or platelets spread on supportive adhesive ligands. Objective: To study assembly of plasma fibronectin by LPA-activated platelets adherent to LN-111 via ,6,1 integrin. Results: Platelets adherent to LN-111-bound plasma fibronectin or its N-terminal 70 kD fragment in fibrillar arrays at the periphery of spread platelets under static but not shear conditions. Formation of fibronectin arrays under static conditions was inhibited by co-incubation with the N-terminal 70 kD fragment or with a 49-amino acid peptide that binds to the N-terminal region of fibronectin. Approximately 7000 fibronectin dimers bound per adherent platelet with a Kd of 50 nm. Bound 70 kD fragment was readily solubilized with deoxycholate (DOC), whereas bound fibronectin became progressively insoluble. Bound 70 kD fragment became resistant to DOC extraction after treatment with a cell-impermeable, reducible crosslinker. Crosslinked 70 kD fragment was found in a high molecular weight complex. As with fibroblasts, signaling molecules modulating actin cytoskeletal organization controlled expression of binding sites for the N-terminal 70 kD region of fibronectin on adherent platelets. Conclusions: These results indicate that platelets adherent to LN-111 via ,6,1 support subsequent assembly of fibronectin, but possibly only under conditions of intermittent or stagnant blood flow. [source] Obestatin , a ghrelin-associated peptide that does not hold its promise to suppress food intake and motilityNEUROGASTROENTEROLOGY & MOTILITY, Issue 3 2007G. Gourcerol Abstract, Ghrelin is a gut peptide well established to induce prokinetic and appetite stimulatory actions. Obestatin is a novel 23-amino acid peptide derived from the processing of the ghrelin gene. The peptide name was in keeping with its initially reported actions to suppress food intake and digestive motility and to antagonize ghrelin's stimulatory effect through interaction with the orphan GPR-39 receptor. However, subsequently, these findings have been questioned because obestatin actions to reduce food intake and to inhibit gastrointestinal (GI) motility in vivo and in vitro have not been reproduced by several groups. Furthermore, while GPR-39 appears to be involved in gut motor functions, convergent reports showed that obestatin is not the cognate ligand for this receptor. In light of recent controversy over the effects of obestatin, the present findings from De Smet et al. provides additional evidence that obestatin does not influence food intake and GI motility in vivo and in vitro. Taken together, existing reports curtail the initial promise that obestatin is a new regulator of appetite and digestive motility. Therefore, it is proposed to rename obestatin as ghrelin-associated peptide. [source] Familial British dementia (FBD): a cerebral amyloidosis with systemic amyloid depositionNEUROPATHOLOGY & APPLIED NEUROBIOLOGY, Issue 2 2002J. L. Holton Introduction:, FBD is an autosomal dominant disease with neuropathological similarities to Alzheimer's disease (AD) as it is characterized by amyloid angiopathy, parenchymal amyloid plaque deposition and neurofibrillary degeneration. FBD is associated with a stop codon mutation in the BRI2 gene encoding a type II transmembrane protein, BriPP. Mutation results in an extended precursor protein, ABriPP, from which a C-terminal 34 amino acid peptide (ABri) is generated by furin-like proteolytic cleavage and deposited as amyloid and preamyloid in the central nervous system. Despite the morphological parallels with AD the sequences of the amyloidogenic peptides, ABri in FBD and A, in AD, are completely different. We examined systemic tissues in FBD for ABri deposition. Materials and methods:, Immunohistochemistry using an ABri-specific antibody, Ab338, counterstained with Thioflavin S and Ab338 immuno-electron microscopy identified ABri deposits and determined whether these were amyloid or preamyloid in nature. Results:, Amyloid bearing blood vessels stained positively for ABri in myocardium, uterus, bladder, spleen, pancreas, lung and skeletal muscle. ABri was also identified in either amyloid or preamyloid conformation in the parenchyma of myocardium, adrenal, pancreas and skeletal muscle. Conclusion:, This study demonstrates that FBD is the first described cerebral amyloidosis with neurofibrillary pathology and dementia to be accompanied by systemic amyloid deposition. [source] Synthesis and NMR solution structure of an ,-helical hairpin stapled with two disulfide bridgesPROTEIN SCIENCE, Issue 5 2000Philippe Barthe Abstract Helical coiled-coils and bundles are some of the most common structural motifs found in proteins. Design and synthesis of ,-helical motifs may provide interesting scaffolds that can be useful as host structures to display functional sites, thus allowing the engineering of novel functional miniproteins. We have synthesized a 38-amino acid peptide, ,2p8, encompassing the ,-helical hairpin present in the structure of p8MTCP1, as an ,-helical scaffold particularly promising for its stability and permissiveness of sequence mutations. The three-dimensional structure of this peptide has been solved using homonuclear two-dimensional NMR techniques at 600 MHz. After sequence specific assignment, a total of 285 distance and 29 dihedral restraints were collected. The solution structure of ,2p8 is presented as a set of 30 DIANA structures, further refined by restrained molecular dynamics, using simulated annealing protocol with the AMBER force field. The RMSD values for the backbone and all heavy atoms are 0.65 ± 0.25 and 1.51 ± 0.21 Å, respectively. Excised from its protein context, the ,-hairpin keeps its native structure: an ,-helical coiled-coil, similar to that found in superhelical structures, with two helices spanning residues 4-16 and 25,36, and linked by a short loop. This motif is stabilized by two interhelical disulfide bridges and several hydrophobic interactions at the helix interface, leaving most of its solvent-exposed surface available for mutation. This ,-helical hairpin, easily amenable to synthetic chemistry and biological expression system, may represent a stable and versatile scaffold to display new functional sites and peptide libraries. [source] Proteomic analysis of spore wall proteins and identification of two spore wall proteins from Nosema bombycis (Microsporidia)PROTEINS: STRUCTURE, FUNCTION AND BIOINFORMATICS, Issue 12 2008Zhengli Wu Abstract Microsporidia are fungal-like unicellular eukaryotes which develop as obligate intracellular parasites. They differentiate into resistant spores that are protected by a thick spore wall composed of a glycoprotein-rich outer layer or exospore and a chitin-rich inner layer or endospore. In this study performed on the silkworm pathogen Nosema bombycis, we analyzed the spore wall proteins (SWPs) by proteomic-based approaches, MALDI-TOF MS and LC-MS/MS, and 14 hypothetical spore wall proteins (HSWPs) or peptides were obtained in total. Furthermore, we have examined the SWPs by SDS-PAGE and three main spore wall peptides were detected with molecular weights of 32.7,kDa (SWP32), 30.4,kDa (SWP30), and 25.3,kDa (SWP25), respectively. By N-terminal amino acid residue sequencing, and searching the genomic DNA shotgun database of N. bombycis, the complete ORFs of SWP30 and SWP32 were obtained, which encode for a 278- and a 316-amino acid peptide, respectively. Mouse polyclonal antibodies were raised against SWP30 and SWP32 recombinant proteins produced in Escherichia coli, and the results of indirect immunofluorescence assay (IFA) and immunoelectron microscopy (IEM) analyses indicated SWP30 to be an endosporal protein while SWP32 was shown to be an exosporal protein. Both SWP30 and SWP32 are included in the 14 HSWPs identified by MS, confirming the results of the proteomic-based approaches. (GenBankÔ, EMBL and DDBJ accession numbers: NbHSWP1,NbHSWP12, accession no. EF683101,EF683112. NbHSWP13 and NbHSWP14, accession no. EU179719 and EU179720). [source] Association between neuropeptide Y gene and its receptor Y1 gene and methamphetamine dependencePSYCHIATRY AND CLINICAL NEUROSCIENCES, Issue 3 2009Yuko Okahisa md Aims:, Neuropeptide Y (NPY) is a 36-amino acid peptide that is widely distributed in the brain, adrenal medulla, and sympathetic nervous system. Several lines of evidence suggest a possible involvement of the NPY system in the physiological effects of several classes of abused substances including alcohol, phencyclidine, cocaine, and marijuana and in endogenous psychosis. Accordingly, it was hypothesized that the NPY system may also be involved in methamphetamine dependence or psychosis. Methods:, The single nucleotide polymorphisms rs16147 of the NPY gene (,485C>T) and rs7687423 of the NPY receptor Y1 (NPY1R) gene were analyzed in 222 patients with methamphetamine dependence and psychosis and 288 age- and gender-matched controls. Results:, Genotypic distribution of the NPY1R gene showed a significant association with methamphetamine dependence and psychosis (P = 0.04), whereas the NPY gene had no significant association with them. Conclusion:, It is possible that genetic variants of the NPY1R gene affect the NPY-NPY receptor type Y1 signaling system in the brain, which may result in susceptibility to methamphetamine dependence or the development of methamphetamine psychosis, but the present findings need to be confirmed on replication. [source] Species differences in bradykinin receptor-mediated responses of the airwaysAUTONOMIC & AUTACOID PHARMACOLOGY, Issue 1 2002K. M. Ellis Summary1 Bradykinin (BK) is a nine amino acid peptide (Arg-Pro-Pro-Gly-Phe-Ser-Pro-Phe-Arg) formed from the plasma precursor kininogen during inflammation and tissue injury. The actions of BK are mediated by G protein-coupled cell surface receptors, designated B1 and B2. 2 BK has a plethora of effects in the airways including bronchoconstriction, bronchodilation, stimulation of cholinergic and sensory nerves, mucus secretion, cough and oedema resulting from promotion of microvascular leakage. These airway effects are mediated in the main by the B2 receptor subtype. 3 BK acts mainly indirectly, primarily through airway nerve activation, but also by the release of prostanoids, thromboxanes and nitric oxide (NO). 4 Airway responses to BK have been studied in detail in guinea-pigs, mice, sheep and rats. This review describes the effects of BK in these species and draws comparison with its effects in normal humans and patients with respiratory diseases. 5 Despite its many and varied effects in the airways of animals and man, the exact contribution of BK to airways disease remains unclear. [source] Structure,activity studies on high affinity NOP-active hexapeptidesCHEMICAL BIOLOGY & DRUG DESIGN, Issue 3 2004A.K. Judd Abstract:, Nociceptin/orphanin FQ (N/OFQ) is a 17 amino acid peptide that is the endogenous ligand for the G-protein coupled receptor ORL1 (NOP), a member of the opioid receptor family. Although it is clear that this receptor system is involved in a variety of physiologic functions, including analgesia, the precise actions of N/OFQ remain largely uncharacterized. One reason for this has been limited number of high-affinity ligands to NOP, and particularly the lack of availability of useful specific antagonists. Herein, we describe the pharmacologic activity of a series of modified amino acid containing modifications of the hexapeptide Ac-RYYRWR-NH2, with high affinity for NOP. These compounds were tested for binding affinity using [3H]N/OFQ binding to human NOP in CHO cells, and functional activity by measuring stimulation of [35S]GTP,S-binding in CHO cell membranes. These studies suggest that each Arg of the hexapeptide is required to maintain high-binding affinity. The peptide maintains high affinity if the Tyr2 or Tyr3 are modified, but at least one of these residues must maintain its hydroxyl group or there is a large decrease in intrinsic activity of the peptide. [source] IR/Raman spectroscopy and DFT calculations of cyclic di-amino acid peptides.JOURNAL OF RAMAN SPECTROSCOPY, Issue 11 2009Part III: comparison of solid state, solution structures of cyclo(L -Ser- L -Ser) Abstract B3-LYP/cc-pVDZ calculations of the gas-phase structure and vibrational spectra of the isolated molecule cyclo(L -Ser- L -Ser), a cyclic di-amino acid peptide (CDAP), were carried out by assuming C2 symmetry. It is predicted that the minimum-energy structure is a boat conformation for the diketopiperazine (DKP) ring with both L -seryl side chains being folded slightly above the ring. An additional structure of higher energy (15.16 kJ mol,1) has been calculated for a DKP ring with a planar geometry, although in this case two fundamental vibrations have been calculated with imaginary wavenumbers. The reported X-ray crystallographic structure of cyclo(L -Ser- L -Ser), shows that the DKP ring displays a near-planar conformation, with both the two L -seryl side chains being folded above the ring. It is hypothesized that the crystal packing forces constrain the DKP ring in a planar conformation and it is probable that the lower energy boat conformation may prevail in the aqueous environment. Raman scattering and Fourier-transform infrared (FT-IR) spectra of solid state and aqueous solution samples of cyclo(L -Ser- L -Ser) are reported and discussed. Vibrational band assignments have been made on the basis of comparisons with the calculated vibrational spectra and band wavenumber shifts upon deuteration of labile protons. The experimental Raman and IR results for solid-state samples show characteristic amide I vibrations which are split (Raman: 1661 and 1687 cm,1, IR: 1666 and 1680 cm,1), possibly due to interactions between molecules in a crystallographic unit cell. The cis amide I band is differentiated by its deuterium shift of ,30 cm,1, which is larger than that previously reported for trans amide I deuterium shifts. A cis amide II mode has been assigned to a Raman band located at 1520 cm,1. The occurrence of this cis amide II mode at a wavenumber above 1500 cm,1 concurs with results of previously examined CDAP molecules with low molecular weight substituents on the C, atoms, and is also indicative of a relatively unstrained DKP ring. Copyright © 2009 John Wiley & Sons, Ltd. [source] Diastereomeric differentiation of norbornene amino acid peptides by electrospray ionization tandem mass spectrometryRAPID COMMUNICATIONS IN MASS SPECTROMETRY, Issue 18 2009B. Raju A new class of diastereomeric pairs of non-natural amino acid peptides derived from butyloxycarbonyl (Boc-)protected cis- (2S,3R)- and trans- (2S,3S) -, -norbornene amino acids including a monomeric pair have been investigated by electrospray ionization (ESI) tandem mass spectrometry using quadrupole time-of-flight (Q-TOF) and ion-trap mass spectrometers. The protonated cis -BocN- , -nbaa (2S,3R) (1) (,nbaa,=,, -norbornene amino acid) eliminates the Boc group to form [M+H,Boc+H]+, whereas an additional ion [M+H,C4H8]+ is formed from trans -BocN- , -nbaa (2S,3S) (2). Similarly, it is observed that the peptide diastereomers (di-, tri- and tetra-), with cis -BocN- , -nbaa (2S,3R)- at the N-terminus, initially eliminate the Boc group to form [M+H,Boc+H]+ which undergo further fragmentation to give a set of product ions that are different for the peptides with trans -BocN- , -nbaa (2S,3S)- at the N-terminus. Thus the Boc group fragments differently depending on the configuration of the amino acid present at the N-terminus. It is also observed that the peptide bond cleavage in these peptides is less favoured and most of the product ions are formed due to retro-Diels-Alder fragmentation. Interestingly, sodium-cationized peptide diastereomers mainly yield a series of retro-Diels-Alder fragment ions which are different for each diastereomer as they are formed starting from [M+Na,Boc+H]+ in peptides with cis -BocN- , -nbaa (2S,3R)- at the N-terminus, and [M+Na,C4H8]+ in peptides with trans -BocN- , -nbaa (2S,3S)- at the N-terminus. All these results clearly indicate that these diastereomeric pairs of peptides yield characteristic product ions which help distinguish the isomers. Copyright © 2009 John Wiley & Sons, Ltd. [source] Weak interactions and molecular recognition in systems involving electron transfer proteinsTHE CHEMICAL RECORD, Issue 4 2001Shun Hirota Abstract Electrostatic interactions and other weak interactions between amino acid side chains on protein surfaces play important roles in molecular recognition, and the mechanism of their intermolecular interactions has gained much interest. We established that charged peptides are useful for investigating the molecular recognition character of proteins and their molecular interaction induced structural changes. Positively charged lysine peptides competitively inhibited electron transfer from reduced cytochrome f (cyt f) or cytochrome c (cyt c) to oxidized plastocyanin (PC), due to neutralization of the negatively charged site of PC by formation of PC,lysine peptide complexes. Lysine peptides also inhibited electron transfer from cyt c to cytochrome c peroxidase. Likewise, negatively charged aspartic acid peptides interacted with the positively charged sites of cyt f and cyt c, and competitively inhibited electron transfer from reduced cyt f or cyt c to oxidized PC and from [Fe(CN)6]4, to oxidized cyt c. Changes in the geometry and a shift to a higher redox potential of the active site Cu of PC on oligolysine binding were detected by spectroscopic and electrochemical measurements, owing to the absence of absorption in the visible region for lysine peptides. Structural and redox potential changes were also observed for cyt f and cyt c by interaction with aspartic acid peptides. ©2001 John Wiley & Sons, Inc. and The Japan Chemical Journal Forum Chem Rec 1:290,299, 2001 [source] | ||||||||||||||||